HSPA1L report

I. Expression across cell types

Insufficient scRNA-seq data for expression of HSPA1L at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of HSPA1L at tissue level.

III. Associated gene sets

GO_0007339Biological processbinding of sperm to zona pellucida
GO_0006986Biological processresponse to unfolded protein
GO_0042026Biological processprotein refolding
GO_1903955Biological processpositive regulation of protein targeting to mitochondrion
GO_0051085Biological processchaperone cofactor-dependent protein refolding
GO_0002199Cellular componentzona pellucida receptor complex
GO_0005654Cellular componentnucleoplasm
GO_0072562Cellular componentblood microparticle
GO_0005829Cellular componentcytosol
GO_0008180Cellular componentCOP9 signalosome
GO_0005759Cellular componentmitochondrial matrix
GO_0005737Cellular componentcytoplasm
GO_0044297Cellular componentcell body
GO_0005634Cellular componentnucleus
GO_0044183Molecular functionprotein folding chaperone
GO_0031072Molecular functionheat shock protein binding
GO_0031625Molecular functionubiquitin protein ligase binding
GO_0051082Molecular functionunfolded protein binding
GO_0140662Molecular functionATP-dependent protein folding chaperone
GO_0005524Molecular functionATP binding
GO_0005515Molecular functionprotein binding
GO_0016887Molecular functionATP hydrolysis activity

IV. Literature review

[source]
Gene nameHSPA1L
Protein nameHeat shock 70 kDa protein 1-like
Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa protein 1-Hom) (HSP70-Hom)
Synonyms
DescriptionFUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release . Positive regulator of PRKN translocation to damaged mitochondria . .

AccessionsENST00000417601.2
Q53FA3
P34931
ENST00000426095.2
ENST00000383390.4
ENST00000375654.5
ENST00000456772.2